GenomeNet

Database: UniProt
Entry: P68363
LinkDB: P68363
Original site: P68363 
ID   TBA1B_HUMAN             Reviewed;         451 AA.
AC   P68363; P04687; P05209; Q27I68; Q8WU19;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   22-APR-2020, entry version 171.
DE   RecName: Full=Tubulin alpha-1B chain;
DE   AltName: Full=Alpha-tubulin ubiquitous;
DE   AltName: Full=Tubulin K-alpha-1;
DE   AltName: Full=Tubulin alpha-ubiquitous chain;
DE   Contains:
DE     RecName: Full=Detyrosinated tubulin alpha-1B chain;
GN   Name=TUBA1B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Keratinocyte;
RX   PubMed=6646120; DOI=10.1128/mcb.3.10.1738;
RA   Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.;
RT   "Expression of human alpha-tubulin genes: interspecies conservation of 3'
RT   untranslated regions.";
RL   Mol. Cell. Biol. 3:1738-1745(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   de Hostos E.L.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Li Q., Liu L., Ma S.;
RT   "Gene response of gangliocytes stimulated by Herpes simplex virus type 1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, Colon, Eye, Kidney, Lung, Muscle, Placenta, Prostate, Skin,
RC   and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 41-60; 65-79; 113-121; 230-280; 312-320; 327-336;
RP   340-370; 374-390; 395-401 AND 403-422, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 41-79; 65-79; 85-121; 125-164; 216-304; 312-370 AND
RP   374-451, PHOSPHORYLATION AT SER-48 AND SER-232, METHYLATION AT ARG-339, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 353-370 AND 395-401.
RC   TISSUE=Brain;
RX   PubMed=8619814; DOI=10.1006/bbrc.1996.0211;
RA   Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J.;
RT   "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in
RT   vitro and associate with amyloid deposits of familial cerebral amyloid
RT   angiopathy, British type.";
RL   Biochem. Biophys. Res. Commun. 219:238-242(1996).
RN   [8]
RP   PROTEIN SEQUENCE OF 439-451, AND NITRATION AT TYR-451.
RX   PubMed=10339593; DOI=10.1073/pnas.96.11.6365;
RA   Eiserich J.P., Estevez A.G., Bamberg T.V., Ye Y.Z., Chumley P.H.,
RA   Beckman J.S., Freeman B.A.;
RT   "Microtubule dysfunction by posttranslational nitrotyrosination of alpha-
RT   tubulin: a nitric oxide-dependent mechanism of cellular injury.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6365-6370(1999).
RN   [9]
RP   GLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA   Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
RN   [10]
RP   ACETYLATION AT LYS-40.
RX   PubMed=24906155; DOI=10.1016/j.cell.2014.03.061;
RA   Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L.,
RA   Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.;
RT   "Molecular basis for age-dependent microtubule acetylation by tubulin
RT   acetyltransferase.";
RL   Cell 157:1405-1415(2014).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   DETYROSINATION.
RX   PubMed=25908662; DOI=10.1126/science.aaa5175;
RA   Barisic M., Silva e Sousa R., Tripathy S.K., Magiera M.M., Zaytsev A.V.,
RA   Pereira A.L., Janke C., Grishchuk E.L., Maiato H.;
RT   "Mitosis. Microtubule detyrosination guides chromosomes during mitosis.";
RL   Science 348:799-803(2015).
RN   [13]
RP   GLUTAMYLATION.
RX   PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
RA   Valenstein M.L., Roll-Mecak A.;
RT   "Graded control of microtubule severing by tubulin glutamylation.";
RL   Cell 164:911-921(2016).
RN   [14]
RP   METHYLATION AT LYS-40.
RX   PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
RA   Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
RA   Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
RA   Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
RT   "Dual chromatin and cytoskeletal remodeling by SETD2.";
RL   Cell 166:950-962(2016).
RN   [15]
RP   TYROSINATION.
RX   PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
RA   Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
RT   "Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
RT   initiation of dynein-driven transport in neurons.";
RL   Cell Rep. 14:2637-2652(2016).
RN   [16]
RP   DETYROSINATION.
RX   PubMed=29146869; DOI=10.1126/science.aao5676;
RA   Nieuwenhuis J., Adamopoulos A., Bleijerveld O.B., Mazouzi A., Stickel E.,
RA   Celie P., Altelaar M., Knipscheer P., Perrakis A., Blomen V.A.,
RA   Brummelkamp T.R.;
RT   "Vasohibins encode tubulin detyrosinating activity.";
RL   Science 358:1453-1456(2017).
RN   [17]
RP   STRUCTURE BY NMR OF 416-451 IN COMPLEX WITH CLIP1.
RX   PubMed=17563362; DOI=10.1073/pnas.0703876104;
RA   Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K.,
RA   Hakoshima T.;
RT   "Structural basis for tubulin recognition by cytoplasmic linker protein 170
RT   and its autoinhibition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC       two moles of GTP, one at an exchangeable site on the beta chain and one
CC       at a non-exchangeable site on the alpha chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC       hollow water-filled tube with an outer diameter of 25 nm and an inner
CC       diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC       form protofilaments running lengthwise along the microtubule wall with
CC       the beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells. {ECO:0000269|PubMed:17563362}.
CC   -!- INTERACTION:
CC       P68363; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-487083, EBI-741181;
CC       P68363; Q8AZK7: EBNA-LP; Xeno; NbExp=3; IntAct=EBI-487083, EBI-1185167;
CC       P68363; Q13509: TUBB3; NbExp=3; IntAct=EBI-487083, EBI-350989;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P68363-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P68363-2; Sequence=VSP_055764;
CC   -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC       resulting in polyglutamate chains on the gamma-carboxyl group
CC       (PubMed:26875866). Polyglutamylation plays a key role in microtubule
CC       severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC       on microtubules decorated with short polyglutamate tails: severing
CC       activity by SPAST increases as the number of glutamates per tubulin
CC       rises from one to eight, but decreases beyond this glutamylation
CC       threshold (PubMed:26875866). {ECO:0000269|PubMed:26875866}.
CC   -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but
CC       not polyglycylated due to the absence of functional TTLL10 in human.
CC       Monoglycylation is mainly limited to tubulin incorporated into axonemes
CC       (cilia and flagella). Both polyglutamylation and monoglycylation can
CC       coexist on the same protein on adjacent residues, and lowering
CC       glycylation levels increases polyglutamylation, and reciprocally. The
CC       precise function of monoglycylation is still unclear (Probable).
CC       {ECO:0000305|PubMed:19524510}.
CC   -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC       microtubule lumen. This modification has been correlated with increased
CC       microtubule stability, intracellular transport and ciliary assembly.
CC       {ECO:0000269|PubMed:24906155}.
CC   -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
CC       microtubules and is required for normal mitosis and cytokinesis
CC       contributing to genomic stability. {ECO:0000305|PubMed:27518565}.
CC   -!- PTM: Nitration of Tyr-451 is irreversible and interferes with normal
CC       dynein intracellular distribution. {ECO:0000269|PubMed:10339593}.
CC   -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC       and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC       tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase
CC       (TTL), respectively. {ECO:0000269|PubMed:25908662,
CC       ECO:0000269|PubMed:26972003, ECO:0000269|PubMed:29146869}.
CC   -!- PTM: [Tubulin alpha-1B chain]: Tyrosination promotes microtubule
CC       interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC       CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation
CC       of dynein-dynactin motility via interaction with DCTN1, which brings
CC       the dynein-dynactin complex into contact with microtubules
CC       (PubMed:26972003). In neurons, tyrosinated tubulins mediate the
CC       initiation of retrograde vesicle transport (By similarity).
CC       {ECO:0000250|UniProtKB:P05213, ECO:0000250|UniProtKB:Q71U36,
CC       ECO:0000269|PubMed:26972003}.
CC   -!- PTM: [Detyrosinated tubulin alpha-1B chain]: Detyrosination is involved
CC       in metaphase plate congression by guiding chromosomes during mitosis:
CC       detyrosination promotes interaction with CENPE, promoting pole-proximal
CC       transport of chromosomes toward the equator (PubMed:25908662).
CC       Detyrosination increases microtubules-dependent mechanotransduction in
CC       dystrophic cardiac and skeletal muscle. In cardiomyocytes,
CC       detyrosinated microtubules are required to resist to contractile
CC       compression during contraction: detyrosination promotes association
CC       with desmin (DES) at force-generating sarcomeres, leading to buckled
CC       microtubules and mechanical resistance to contraction (By similarity).
CC       {ECO:0000250|UniProtKB:P05213, ECO:0000269|PubMed:25908662}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
DR   EMBL; K00558; AAA91576.1; -; mRNA.
DR   EMBL; AF081484; AAC31959.1; -; mRNA.
DR   EMBL; DQ400107; ABD60581.1; -; mRNA.
DR   EMBL; BC000696; AAH00696.1; -; mRNA.
DR   EMBL; BC001128; AAH01128.1; -; mRNA.
DR   EMBL; BC006379; AAH06379.1; -; mRNA.
DR   EMBL; BC006481; AAH06481.1; -; mRNA.
DR   EMBL; BC008659; AAH08659.1; -; mRNA.
DR   EMBL; BC009314; AAH09314.1; -; mRNA.
DR   EMBL; BC009509; AAH09509.1; -; mRNA.
DR   EMBL; BC009512; AAH09512.1; -; mRNA.
DR   EMBL; BC009513; AAH09513.1; -; mRNA.
DR   EMBL; BC010494; AAH10494.1; -; mRNA.
DR   EMBL; BC011572; AAH11572.1; -; mRNA.
DR   EMBL; BC015883; AAH15883.1; -; mRNA.
DR   EMBL; BC017004; AAH17004.1; -; mRNA.
DR   EMBL; BC021564; AAH21564.1; -; mRNA.
DR   EMBL; BC030820; AAH30820.1; -; mRNA.
DR   EMBL; BC071904; AAH71904.1; -; mRNA.
DR   CCDS; CCDS31792.1; -. [P68363-1]
DR   PIR; I77403; I77403.
DR   RefSeq; NP_006073.2; NM_006082.2. [P68363-1]
DR   PDB; 2E4H; NMR; -; B=416-451.
DR   PDB; 5IJ0; EM; 3.80 A; A=1-437.
DR   PDB; 5IJ9; EM; 3.70 A; A=1-437.
DR   PDB; 5N5N; EM; 4.00 A; G/H/I/J/K/L=1-437.
DR   PDB; 6E7B; EM; 3.50 A; A=1-437.
DR   PDB; 6E7C; EM; 3.65 A; A=1-437.
DR   PDB; 6I2I; EM; 3.60 A; A=1-451.
DR   PDB; 6J4V; X-ray; 2.10 A; C=431-451.
DR   PDB; 6QUS; EM; 3.70 A; O/X=1-451.
DR   PDB; 6QUY; EM; 3.80 A; A/C=1-451.
DR   PDB; 6QVE; EM; 3.70 A; A/C=1-451.
DR   PDB; 6QVJ; EM; 3.80 A; O/X=1-451.
DR   PDB; 6S8L; X-ray; 1.80 A; A=1-451.
DR   PDBsum; 2E4H; -.
DR   PDBsum; 5IJ0; -.
DR   PDBsum; 5IJ9; -.
DR   PDBsum; 5N5N; -.
DR   PDBsum; 6E7B; -.
DR   PDBsum; 6E7C; -.
DR   PDBsum; 6I2I; -.
DR   PDBsum; 6J4V; -.
DR   PDBsum; 6QUS; -.
DR   PDBsum; 6QUY; -.
DR   PDBsum; 6QVE; -.
DR   PDBsum; 6QVJ; -.
DR   PDBsum; 6S8L; -.
DR   SMR; P68363; -.
DR   BioGrid; 115651; 186.
DR   CORUM; P68363; -.
DR   IntAct; P68363; 77.
DR   MINT; P68363; -.
DR   STRING; 9606.ENSP00000336799; -.
DR   ChEMBL; CHEMBL3797010; -.
DR   DrugBank; DB07574; 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE.
DR   DrugBank; DB05147; CYT997.
DR   DrugBank; DB01873; Epothilone D.
DR   DrugBank; DB03010; Patupilone.
DR   DrugCentral; P68363; -.
DR   CarbonylDB; P68363; -.
DR   iPTMnet; P68363; -.
DR   MetOSite; P68363; -.
DR   PhosphoSitePlus; P68363; -.
DR   SwissPalm; P68363; -.
DR   BioMuta; TUBA1B; -.
DR   DMDM; 55977474; -.
DR   OGP; P68363; -.
DR   SWISS-2DPAGE; P68363; -.
DR   EPD; P68363; -.
DR   jPOST; P68363; -.
DR   MassIVE; P68363; -.
DR   MaxQB; P68363; -.
DR   PaxDb; P68363; -.
DR   PeptideAtlas; P68363; -.
DR   PRIDE; P68363; -.
DR   ProteomicsDB; 57533; -. [P68363-1]
DR   TopDownProteomics; P68363-1; -. [P68363-1]
DR   ABCD; P68363; -.
DR   Antibodypedia; 3156; 620 antibodies.
DR   DNASU; 10376; -.
DR   Ensembl; ENST00000336023; ENSP00000336799; ENSG00000123416. [P68363-1]
DR   GeneID; 10376; -.
DR   KEGG; hsa:10376; -.
DR   UCSC; uc001rtm.4; human. [P68363-1]
DR   CTD; 10376; -.
DR   DisGeNET; 10376; -.
DR   GeneCards; TUBA1B; -.
DR   HGNC; HGNC:18809; TUBA1B.
DR   HPA; ENSG00000123416; Low tissue specificity.
DR   MIM; 602530; gene.
DR   neXtProt; NX_P68363; -.
DR   OpenTargets; ENSG00000123416; -.
DR   PharmGKB; PA162407332; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   eggNOG; COG5023; LUCA.
DR   GeneTree; ENSGT00950000182825; -.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; P68363; -.
DR   KO; K07374; -.
DR   OMA; VDNEACY; -.
DR   OrthoDB; 514396at2759; -.
DR   PhylomeDB; P68363; -.
DR   TreeFam; TF300314; -.
DR   Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR   Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR   Reactome; R-HSA-190861; Gap junction assembly.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR   Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR   Reactome; R-HSA-437239; Recycling pathway of L1.
DR   Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR   Reactome; R-HSA-5617833; Cilium Assembly.
DR   Reactome; R-HSA-5620924; Intraflagellar transport.
DR   Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR   Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR   Reactome; R-HSA-9646399; Aggrephagy.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-HSA-983189; Kinesins.
DR   SIGNOR; P68363; -.
DR   ChiTaRS; TUBA1B; human.
DR   EvolutionaryTrace; P68363; -.
DR   GeneWiki; TUBA1B; -.
DR   GenomeRNAi; 10376; -.
DR   Pharos; P68363; Tchem.
DR   PRO; PR:P68363; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P68363; protein.
DR   Bgee; ENSG00000123416; Expressed in anterior cingulate cortex and 122 other tissues.
DR   ExpressionAtlas; P68363; baseline and differential.
DR   Genevisible; P68363; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0051301; P:cell division; TAS:BHF-UCL.
DR   GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   DisProt; DP02251; -.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR037103; Tubulin/FtsZ_C_sf.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
KW   Microtubule; Nitration; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..451
FT                   /note="Tubulin alpha-1B chain"
FT                   /id="PRO_0000048108"
FT   CHAIN           1..450
FT                   /note="Detyrosinated tubulin alpha-1B chain"
FT                   /evidence="ECO:0000305|PubMed:25908662,
FT                   ECO:0000305|PubMed:29146869"
FT                   /id="PRO_0000437384"
FT   NP_BIND         142..148
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
FT   SITE            451
FT                   /note="Involved in polymerization"
FT   MOD_RES         40
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27518565"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24906155"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|Ref.6"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|Ref.6"
FT   MOD_RES         282
FT                   /note="Nitrated tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P68373"
FT   MOD_RES         339
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|Ref.6"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68373"
FT   MOD_RES         445
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P68369"
FT   MOD_RES         451
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10339593"
FT   CROSSLNK        326
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        370
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   VAR_SEQ         108..223
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055764"
FT   CONFLICT        131
FT                   /note="G -> R (in Ref. 1; AAA91576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="E -> D (in Ref. 1; AAA91576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="R -> G (in Ref. 1; AAA91576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="S -> T (in Ref. 1; AAA91576)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..9
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           10..28
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           48..51
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          53..55
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          61..63
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          65..72
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           73..80
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   TURN            82..86
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           89..91
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          92..94
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           103..107
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           111..113
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           115..127
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          134..143
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           144..160
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          165..172
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           175..177
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           183..194
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   TURN            195..197
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          199..205
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           206..215
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           224..243
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           252..259
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          261..264
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          269..273
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           288..293
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           294..296
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           298..300
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          301..303
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           307..309
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          312..322
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           325..336
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          352..356
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          372..381
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           382..384
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           385..399
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   TURN            400..404
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           405..409
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   TURN            410..412
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           416..435
FT                   /evidence="ECO:0000244|PDB:6S8L"
SQ   SEQUENCE   451 AA;  50152 MW;  94355B4EC2086429 CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
     RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
//
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